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In crystallo observation of active site dynamics and transient metal ion binding within DNA polymerases.

ABSTRACT: DNA polymerases are the enzymatic catalysts that synthesize DNA during DNA replication and repair. Kinetic studies and x-ray crystallography have uncovered the overall kinetic pathway and led to a two-metal-ion dependent catalytic mechanism. Diffusion-based time-resolved crystallography has permitted the visualization of the catalytic reaction at atomic resolution and made it possible to capture transient events and metal ion binding that have eluded static polymerase structures. This review discusses past static structures and recent time-resolved structures that emphasize the crucial importance of primer alignment and different metal ions binding during catalysis and substrate discrimination.

SUBMITTER: Chang C

PROVIDER: S-EPMC10275647 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature

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In crystallo observation of active site dynamics and transient metal ion binding within DNA polymerases.

Chang Caleb C Zhou Grace G Gao Yang Y

Structural dynamics (Melville, N.Y.) 20230501 3

DNA polymerases are the enzymatic catalysts that synthesize DNA during DNA replication and repair. Kinetic studies and x-ray crystallography have uncovered the overall kinetic pathway and led to a two-metal-ion dependent catalytic mechanism. Diffusion-based time-resolved crystallography has permitted the visualization of the catalytic reaction at atomic resolution and made it possible to capture transient events and metal ion binding that have eluded static polymerase structures. This review dis ...[more]

PMID: 37333512

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